OASL2 Inhibitors

Chemical inhibitors of OASL2 function through various molecular interactions that lead to the inhibition of the protein's enzymatic or binding activities. Zn2+, Cu2+, Hg2+, Pb2+, and Cd2+ are metal ions that can disrupt OASL2 function by different mechanisms. Zn2+ can bind to the oligoadenylate synthetase domain, which is crucial for the protein's enzymatic activity, thus directly inhibiting its function. Similarly, Cu2+ competes with essential metal ions for binding sites on OASL2, disrupting its enzymatic activity. Hg2+ ions can bind to thiol groups in OASL2's active site, causing a loss of enzymatic function, while Pb2+ interferes with the RNA-binding capacity of OASL2, inhibiting its function. Cd2+, like Zn2+ and Cu2+, can displace necessary metal cofactors in the catalytic site, leading to inhibition of OASL2's activity.

Suramin, a non-specific binder to nucleotide-binding proteins, can inhibit OASL2 by potentially blocking its activity through non-specific interactions. Polyanions, represented here by polyacrylic acid, can bind to OASL2's RNA-binding domain, hindering its interaction with functional RNAs, which is essential for the protein's activity. Ribavirin, by mimicking the RNA substrate of OASL2, can lead to competitive inhibition, preventing the protein from properly interacting with its actual RNA substrate. Chloroquine and hydroxychloroquine can raise endosomal pH, which in turn can affect the RNA binding or catalytic function of OASL2 within these cellular compartments. Ebselen, by binding to cysteine residues, may disrupt the protein's structure and function, leading to inhibition.